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Calcium in PDB 1tah: The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate

Enzymatic activity of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate

All present enzymatic activity of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate:
3.1.1.3;

Protein crystallography data

The structure of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate, PDB code: 1tah was solved by M.E.M.Noble, A.Cleasby, L.N.Johnson, M.Egmond, L.G.J.Frenken, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 3.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 158.160, 158.640, 63.360, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 22.6

Calcium Binding Sites:

The binding sites of Calcium atom in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate (pdb code 1tah). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate, PDB code: 1tah:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 1tah

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Calcium binding site 1 out of 4 in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca320

b:11.9
occ:1.00
OD2 B:ASP241 2.3 33.5 1.0
OD1 B:ASP287 2.5 72.6 1.0
O B:VAL295 2.6 26.5 1.0
O B:GLN291 2.6 7.0 1.0
CG B:ASP241 3.4 22.4 1.0
CG B:ASP287 3.7 4.8 1.0
C B:VAL295 3.7 5.2 1.0
C B:GLN291 3.8 17.4 1.0
OG B:SER243 4.0 20.1 1.0
OD1 B:ASP241 4.1 18.6 1.0
OD1 B:ASN284 4.3 4.9 1.0
OD2 B:ASP287 4.4 22.7 1.0
CB B:ASP241 4.4 4.0 1.0
OG1 B:THR244 4.4 12.0 1.0
CA B:ARG296 4.4 6.8 1.0
N B:ASP287 4.5 21.9 1.0
N B:ARG296 4.5 25.5 1.0
CA B:ASP287 4.5 21.8 1.0
CB B:VAL295 4.6 2.0 1.0
CA B:VAL295 4.6 2.0 1.0
CB B:ASP287 4.7 2.0 1.0
N B:LEU292 4.8 73.4 1.0
CA B:GLN291 4.9 5.6 1.0
CB B:LEU292 4.9 2.8 1.0
N B:VAL295 4.9 2.0 1.0
O B:LEU292 4.9 7.6 1.0
C B:LEU286 4.9 2.0 1.0
N B:GLN291 5.0 19.0 1.0

Calcium binding site 2 out of 4 in 1tah

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Calcium binding site 2 out of 4 in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca320

b:43.5
occ:1.00
OD2 A:ASP241 2.4 32.8 1.0
OD1 A:ASP287 2.4 71.7 1.0
O A:VAL295 2.5 14.5 1.0
O A:GLN291 2.7 11.7 1.0
CG A:ASP241 3.5 24.1 1.0
C A:VAL295 3.6 2.0 1.0
CG A:ASP287 3.6 10.0 1.0
C A:GLN291 3.9 19.8 1.0
OG A:SER243 4.1 23.4 1.0
OD1 A:ASP241 4.2 23.0 1.0
CA A:ARG296 4.3 13.2 1.0
OD2 A:ASP287 4.3 29.6 1.0
OD1 A:ASN284 4.3 8.2 1.0
N A:ARG296 4.4 25.2 1.0
OG1 A:THR244 4.4 3.2 1.0
CB A:ASP241 4.4 6.2 1.0
CA A:ASP287 4.5 28.4 1.0
N A:ASP287 4.5 25.8 1.0
CB A:VAL295 4.6 9.9 1.0
CA A:VAL295 4.6 5.1 1.0
CB A:ASP287 4.6 2.0 1.0
N A:VAL295 4.9 2.0 1.0
N A:LEU292 4.9 74.8 1.0
CA A:GLN291 4.9 7.5 1.0
C A:LEU286 5.0 2.0 1.0
O A:LEU292 5.0 16.9 1.0

Calcium binding site 3 out of 4 in 1tah

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Calcium binding site 3 out of 4 in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca320

b:8.3
occ:1.00
OD2 C:ASP241 2.4 31.6 1.0
OD1 C:ASP287 2.4 75.5 1.0
O C:VAL295 2.5 18.6 1.0
O C:GLN291 2.9 2.0 1.0
CG C:ASP241 3.5 12.6 1.0
C C:VAL295 3.6 7.7 1.0
CG C:ASP287 3.6 5.7 1.0
C C:GLN291 4.1 18.2 1.0
CA C:ARG296 4.2 6.9 1.0
OD2 C:ASP287 4.2 16.9 1.0
OG C:SER243 4.2 22.1 1.0
OG1 C:THR244 4.2 16.6 1.0
OD1 C:ASP241 4.3 9.0 1.0
N C:ARG296 4.3 24.7 1.0
OD1 C:ASN284 4.3 15.6 1.0
CB C:ASP241 4.4 2.0 1.0
CA C:ASP287 4.6 23.6 1.0
CB C:VAL295 4.6 2.0 1.0
N C:ASP287 4.6 20.6 1.0
CA C:VAL295 4.6 2.0 1.0
CB C:ASP287 4.6 2.0 1.0
N C:VAL295 5.0 8.6 1.0

Calcium binding site 4 out of 4 in 1tah

Go back to Calcium Binding Sites List in 1tah
Calcium binding site 4 out of 4 in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ca320

b:16.8
occ:1.00
OD1 D:ASP287 2.3 69.5 1.0
O D:VAL295 2.5 18.8 1.0
OD2 D:ASP241 2.5 29.8 1.0
O D:GLN291 2.9 2.0 1.0
CG D:ASP287 3.5 2.0 1.0
C D:VAL295 3.5 2.0 1.0
CG D:ASP241 3.6 15.7 1.0
OD2 D:ASP287 4.1 22.7 1.0
CA D:ARG296 4.1 2.0 1.0
C D:GLN291 4.2 12.7 1.0
N D:ARG296 4.2 22.5 1.0
OG1 D:THR244 4.3 15.0 1.0
OG D:SER243 4.3 24.4 1.0
OD1 D:ASN284 4.3 2.0 1.0
OD1 D:ASP241 4.4 16.3 1.0
CB D:ASP241 4.4 2.0 1.0
CA D:ASP287 4.5 17.9 1.0
N D:ASP287 4.5 16.2 1.0
CB D:ASP287 4.5 2.0 1.0
CA D:VAL295 4.6 8.2 1.0
CB D:VAL295 4.6 2.0 1.0
N D:VAL295 5.0 10.4 1.0
CG D:ARG296 5.0 26.8 1.0

Reference:

M.E.Noble, A.Cleasby, L.N.Johnson, M.R.Egmond, L.G.Frenken. The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate. Febs Lett. V. 331 123 1993.
ISSN: ISSN 0014-5793
PubMed: 8405390
DOI: 10.1016/0014-5793(93)80310-Q
Page generated: Tue Jul 8 02:12:00 2025

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